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P98174

- FGD1_HUMAN

UniProt

P98174 - FGD1_HUMAN

Protein

FYVE, RhoGEF and PH domain-containing protein 1

Gene

FGD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 2 (01 Feb 2003)
      Previous versions | rss
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    Functioni

    Activates CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. Plays a role in regulating the actin cytoskeleton and cell shape.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri730 – 79061FYVE-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. guanyl-nucleotide exchange factor activity Source: UniProtKB
    2. metal ion binding Source: UniProtKB-KW
    3. Rho guanyl-nucleotide exchange factor activity Source: InterPro
    4. small GTPase binding Source: UniProtKB

    GO - Biological processi

    1. actin cytoskeleton organization Source: UniProtKB
    2. apoptotic signaling pathway Source: Reactome
    3. cytoskeleton organization Source: UniProtKB
    4. filopodium assembly Source: UniProtKB
    5. multicellular organismal development Source: ProtInc
    6. neurotrophin TRK receptor signaling pathway Source: Reactome
    7. organ morphogenesis Source: ProtInc
    8. positive regulation of apoptotic process Source: Reactome
    9. positive regulation of GTPase activity Source: GOC
    10. regulation of Cdc42 GTPase activity Source: UniProtKB
    11. regulation of cell shape Source: UniProtKB
    12. regulation of small GTPase mediated signal transduction Source: Reactome
    13. signal transduction Source: ProtInc
    14. small GTPase mediated signal transduction Source: Reactome

    Keywords - Molecular functioni

    Guanine-nucleotide releasing factor

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_11051. Rho GTPase cycle.
    REACT_13638. NRAGE signals death through JNK.
    REACT_18407. G alpha (12/13) signalling events.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    FYVE, RhoGEF and PH domain-containing protein 1
    Alternative name(s):
    Faciogenital dysplasia 1 protein
    Rho/Rac guanine nucleotide exchange factor FGD1
    Short name:
    Rho/Rac GEF
    Zinc finger FYVE domain-containing protein 3
    Gene namesi
    Name:FGD1
    Synonyms:FGDY, ZFYVE3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:3663. FGD1.

    Subcellular locationi

    Cytoplasm By similarity. Cell projectionlamellipodium By similarity. Cell projectionruffle By similarity. Cytoplasmcytoskeleton By similarity
    Note: Associated with membrane ruffles and lamellipodia.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoskeleton Source: UniProtKB-SubCell
    3. cytosol Source: Reactome
    4. Golgi apparatus Source: UniProtKB
    5. lamellipodium Source: UniProtKB
    6. ruffle Source: UniProtKB

    Keywords - Cellular componenti

    Cell projection, Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Involvement in diseasei

    Aarskog-Scott syndrome (AAS) [MIM:305400]: A rare multisystemic disorder characterized by disproportionately short stature, and by facial, skeletal and urogenital anomalies. Some patients manifest mental retardation, attention deficit disorder and hyperactivity.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti205 – 2051S → I in AAS. 1 Publication
    VAR_019268
    Natural varianti380 – 3801E → A in AAS. 1 Publication
    VAR_019270
    Natural varianti443 – 4431R → H in AAS. 1 Publication
    VAR_019271
    Natural varianti522 – 5221R → H in AAS. 1 Publication
    VAR_015236
    Natural varianti610 – 6101R → Q in AAS. 1 Publication
    Corresponds to variant rs28935497 [ dbSNP | Ensembl ].
    VAR_015237
    Defects in FGD1 are found in a patient with non-syndromal X-linked mental retardation.

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi305400. phenotype.
    Orphaneti915. Aarskog-Scott syndrome.
    PharmGKBiPA28102.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 961961FYVE, RhoGEF and PH domain-containing protein 1PRO_0000080940Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei48 – 481Phosphoserine1 Publication
    Modified residuei205 – 2051Phosphoserine1 Publication
    Modified residuei365 – 3651Phosphoserine1 Publication
    Modified residuei711 – 7111Phosphothreonine1 Publication
    Modified residuei715 – 7151Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP98174.
    PaxDbiP98174.
    PRIDEiP98174.

    PTM databases

    PhosphoSiteiP98174.

    Expressioni

    Tissue specificityi

    Expressed in fetal heart, brain, lung, kidney and placenta. Less expressed in liver; adult heart, brain, lung, pancreas and skeletal muscle.

    Gene expression databases

    BgeeiP98174.
    CleanExiHS_FGD1.
    GenevestigatoriP98174.

    Organism-specific databases

    HPAiHPA000911.

    Interactioni

    Subunit structurei

    Interacts with DBNL/ABP1 and CTTN. May interact with CCPG1 By similarity. Binds CDC42.By similarity

    Protein-protein interaction databases

    BioGridi108536. 4 interactions.
    MINTiMINT-2805047.
    STRINGi9606.ENSP00000364277.

    Structurei

    3D structure databases

    ProteinModelPortaliP98174.
    SMRiP98174. Positions 316-786, 831-920.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini373 – 561189DHPROSITE-ProRule annotationAdd
    BLAST
    Domaini590 – 689100PH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini821 – 921101PH 2PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi171 – 18717SH3-bindingSequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi7 – 330324Pro-richAdd
    BLAST

    Domaini

    The DH domain is involved in interaction with CCPG1.By similarity

    Sequence similaritiesi

    Contains 1 DH (DBL-homology) domain.PROSITE-ProRule annotation
    Contains 1 FYVE-type zinc finger.PROSITE-ProRule annotation
    Contains 2 PH domains.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri730 – 79061FYVE-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG295069.
    HOGENOMiHOG000220866.
    HOVERGENiHBG007506.
    InParanoidiP98174.
    KOiK05720.
    OMAiLQMPRMP.
    OrthoDBiEOG7C2R0M.
    PhylomeDBiP98174.
    TreeFamiTF316247.

    Family and domain databases

    Gene3Di1.20.900.10. 1 hit.
    2.30.29.30. 2 hits.
    3.30.40.10. 1 hit.
    InterProiIPR000219. DH-domain.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR000306. Znf_FYVE.
    IPR017455. Znf_FYVE-rel.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF01363. FYVE. 1 hit.
    PF00169. PH. 2 hits.
    PF00621. RhoGEF. 1 hit.
    [Graphical view]
    SMARTiSM00064. FYVE. 1 hit.
    SM00233. PH. 2 hits.
    SM00325. RhoGEF. 1 hit.
    [Graphical view]
    SUPFAMiSSF48065. SSF48065. 1 hit.
    PROSITEiPS50010. DH_2. 1 hit.
    PS50003. PH_DOMAIN. 2 hits.
    PS50178. ZF_FYVE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P98174-1 [UniParc]FASTAAdd to Basket

    « Hide

    MHGHRAPGGA GPSEPEHPAT NPPGAAPPAC ADSDPGASEP GLLARRGSGS    50
    ALGGPLDPQF VGPSDTSLGA APGHRVLPCG PSPQHHRALR FSYHLEGSQP 100
    RPGLHQGNRI LVKSLSLDPG QSLEPHPEGP QRLRSDPGPP TETPSQRPSP 150
    LKRAPGPKPQ VPPKPSYLQM PRMPPPLEPI PPPPSRPLPA DPRVAKGLAP 200
    RAEASPSSAA VSSLIEKFER EPVIVASDRP VPGPSPGPPE PVMLPQPTSQ 250
    PPVPQLPEGE ASRCLFLLAP GPRDGEKVPN RDSGIDSISS PSNSEETCFV 300
    SDDGPPSHSL CPGPPALASV PVALADPHRP GSQEVDSDLE EEDDEEEEEE 350
    KDREIPVPLM ERQESVELTV QQKVFHIANE LLQTEKAYVS RLHLLDQVFC 400
    ARLLEEARNR SSFPADVVHG IFSNICSIYC FHQQFLLPEL EKRMEEWDRY 450
    PRIGDILQKL APFLKMYGEY VKNFDRAVEL VNTWTERSTQ FKVIIHEVQK 500
    EEACGNLTLQ HHMLEPVQRI PRYELLLKDY LLKLPHGSPD SKDAQKSLEL 550
    IATAAEHSNA AIRKMERMHK LLKVYELLGG EEDIVSPTKE LIKEGHILKL 600
    SAKNGTTQDR YLILFNDRLL YCVPRLRLLG QKFSVRARID VDGMELKESS 650
    NLNLPRTFLV SGKQRSLELQ ARTEEEKKDW VQAINSTLLK HEQTLETFKL 700
    LNSTNREDED TPPNSPNVDL GKRAPTPIRE KEVTMCMRCQ EPFNSITKRR 750
    HHCKACGHVV CGKCSEFRAR LVYDNNRSNR VCTDCYVALH GVPGSSPACS 800
    QHTPQRRRSI LEKQASVAAE NSVICSFLHY MEKGGKGWHK AWFVVPENEP 850
    LVLYIYGAPQ DVKAQRSLPL IGFEVGPPEA GERPDRRHVF KITQSHLSWY 900
    FSPETEELQR RWMAVLGRAG RGDTFCPGPT LSEDREMEEA PVAALGATAE 950
    PPESPQTRDK T 961
    Length:961
    Mass (Da):106,561
    Last modified:February 1, 2003 - v2
    Checksum:i30963F7B9931E45C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti10 – 2314AGPSE…ATNPP → RRAFGARTPGHEPA(PubMed:7954831)CuratedAdd
    BLAST
    Sequence conflicti195 – 1951A → G in AAA57004. (PubMed:7954831)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti205 – 2051S → I in AAS. 1 Publication
    VAR_019268
    Natural varianti312 – 3121P → L in non-syndromal X-linked mental retardation. 1 Publication
    Corresponds to variant rs28935498 [ dbSNP | Ensembl ].
    VAR_019269
    Natural varianti380 – 3801E → A in AAS. 1 Publication
    VAR_019270
    Natural varianti443 – 4431R → H in AAS. 1 Publication
    VAR_019271
    Natural varianti522 – 5221R → H in AAS. 1 Publication
    VAR_015236
    Natural varianti610 – 6101R → Q in AAS. 1 Publication
    Corresponds to variant rs28935497 [ dbSNP | Ensembl ].
    VAR_015237

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U11690 mRNA. Translation: AAA57004.1.
    Z85987 Genomic DNA. Translation: CAI42222.1.
    CH471154 Genomic DNA. Translation: EAW93179.1.
    BC034530 mRNA. Translation: AAH34530.1.
    CCDSiCCDS14359.1.
    PIRiA55380.
    RefSeqiNP_004454.2. NM_004463.2.
    UniGeneiHs.709201.

    Genome annotation databases

    EnsembliENST00000375135; ENSP00000364277; ENSG00000102302.
    GeneIDi2245.
    KEGGihsa:2245.
    UCSCiuc004dtg.3. human.

    Polymorphism databases

    DMDMi28202247.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U11690 mRNA. Translation: AAA57004.1 .
    Z85987 Genomic DNA. Translation: CAI42222.1 .
    CH471154 Genomic DNA. Translation: EAW93179.1 .
    BC034530 mRNA. Translation: AAH34530.1 .
    CCDSi CCDS14359.1.
    PIRi A55380.
    RefSeqi NP_004454.2. NM_004463.2.
    UniGenei Hs.709201.

    3D structure databases

    ProteinModelPortali P98174.
    SMRi P98174. Positions 316-786, 831-920.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108536. 4 interactions.
    MINTi MINT-2805047.
    STRINGi 9606.ENSP00000364277.

    Chemistry

    BindingDBi P98174.
    ChEMBLi CHEMBL2862.

    PTM databases

    PhosphoSitei P98174.

    Polymorphism databases

    DMDMi 28202247.

    Proteomic databases

    MaxQBi P98174.
    PaxDbi P98174.
    PRIDEi P98174.

    Protocols and materials databases

    DNASUi 2245.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000375135 ; ENSP00000364277 ; ENSG00000102302 .
    GeneIDi 2245.
    KEGGi hsa:2245.
    UCSCi uc004dtg.3. human.

    Organism-specific databases

    CTDi 2245.
    GeneCardsi GC0XM054488.
    HGNCi HGNC:3663. FGD1.
    HPAi HPA000911.
    MIMi 300546. gene.
    305400. phenotype.
    neXtProti NX_P98174.
    Orphaneti 915. Aarskog-Scott syndrome.
    PharmGKBi PA28102.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG295069.
    HOGENOMi HOG000220866.
    HOVERGENi HBG007506.
    InParanoidi P98174.
    KOi K05720.
    OMAi LQMPRMP.
    OrthoDBi EOG7C2R0M.
    PhylomeDBi P98174.
    TreeFami TF316247.

    Enzyme and pathway databases

    Reactomei REACT_11051. Rho GTPase cycle.
    REACT_13638. NRAGE signals death through JNK.
    REACT_18407. G alpha (12/13) signalling events.

    Miscellaneous databases

    ChiTaRSi FGD1. human.
    GeneWikii FGD1.
    GenomeRNAii 2245.
    NextBioi 9083.
    PROi P98174.
    SOURCEi Search...

    Gene expression databases

    Bgeei P98174.
    CleanExi HS_FGD1.
    Genevestigatori P98174.

    Family and domain databases

    Gene3Di 1.20.900.10. 1 hit.
    2.30.29.30. 2 hits.
    3.30.40.10. 1 hit.
    InterProi IPR000219. DH-domain.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR000306. Znf_FYVE.
    IPR017455. Znf_FYVE-rel.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF01363. FYVE. 1 hit.
    PF00169. PH. 2 hits.
    PF00621. RhoGEF. 1 hit.
    [Graphical view ]
    SMARTi SM00064. FYVE. 1 hit.
    SM00233. PH. 2 hits.
    SM00325. RhoGEF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48065. SSF48065. 1 hit.
    PROSITEi PS50010. DH_2. 1 hit.
    PS50003. PH_DOMAIN. 2 hits.
    PS50178. ZF_FYVE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of the faciogenital dysplasia (Aarskog-Scott syndrome) gene: a putative Rho/Rac guanine nucleotide exchange factor."
      Pasteris N.G., Cadle A., Logie L.J., Porteous M.E.M., Schwartz C.E., Stevenson R.E., Glover T.W., Wilroy R.S., Gorski J.L.
      Cell 79:669-678(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Craniofacial.
    2. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    5. "The faciogenital dysplasia gene product FGD1 functions as a Cdc42Hs-specific guanine-nucleotide exchange factor."
      Zheng Y., Fischer D.J., Santos M.F., Tigyi G., Pasteris N.G., Gorski J.L., Xu Y.
      J. Biol. Chem. 271:33169-33172(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; SER-205; THR-711 AND SER-715, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Two novel mutations confirm FGD1 is responsible for the Aarskog syndrome."
      Schwartz C.E., Gillessen-Kaesbach G., May M., Cappa M., Gorski J.L., Steindl K., Neri G.
      Eur. J. Hum. Genet. 8:869-874(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT AAS HIS-522.
    10. "A mutation in the pleckstrin homology (PH) domain of the FGD1 gene in an Italian family with faciogenital dysplasia (Aarskog-Scott syndrome)."
      Orrico A., Galli L., Falciani M., Bracci M., Cavaliere M.L., Rinaldi M.M., Musacchio A., Sorrentino V.
      FEBS Lett. 478:216-220(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT AAS GLN-610.
    11. "Non-syndromic X-linked mental retardation associated with a missense mutation (P312L) in the FGD1 gene."
      Lebel R.R., May M., Pouls S., Lubs H.A., Stevenson R.E., Schwartz C.E.
      Clin. Genet. 61:139-145(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT NONSYNDROMAL X-LINKED MENTAL RETARDATION LEU-312.
    12. "Phenotypic and molecular characterisation of the Aarskog-Scott syndrome: a survey of the clinical variability in light of FGD1 mutation analysis in 46 patients."
      Orrico A., Galli L., Cavaliere M.L., Garavelli L., Fryns J.-P., Crushell E., Rinaldi M.M., Medeira A., Sorrentino V.
      Eur. J. Hum. Genet. 12:16-23(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS AAS ILE-205; ALA-380 AND HIS-443.

    Entry informationi

    Entry nameiFGD1_HUMAN
    AccessioniPrimary (citable) accession number: P98174
    Secondary accession number(s): Q5H999, Q8N4D9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: February 1, 2003
    Last modified: October 1, 2014
    This is version 148 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3